His-859 Is an Essential Residue for the Activity and pH Dependence of Escherichia coli RTX Toxin α-Hemolysin
Open Access
- 1 June 2002
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 277 (26) , 23223-23229
- https://doi.org/10.1074/jbc.m202028200
Abstract
No abstract availableKeywords
This publication has 18 references indexed in Scilit:
- ABC transporters: bacterial exporters-revisited five years onBiochimica et Biophysica Acta (BBA) - Biomembranes, 1999
- E. coli a-hemolysin: a membrane-active protein toxinBrazilian Journal of Medical and Biological Research, 1998
- Reversible Denaturation, Self-Aggregation, and Membrane Activity of Escherichia coli α-Hemolysin, a Protein Stable in 6 M UreaBiochemistry, 1998
- Calcium-dependent conformation of E. coli α-haemolysin. Implications for the mechanism of membrane insertion and lysisBiochimica et Biophysica Acta (BBA) - Biomembranes, 1998
- Reversible adsorption and nonreversible insertion of Escherichia coli alpha-hemolysin into lipid bilayersBiophysical Journal, 1996
- The RTX toxins of Gram-negative bacterial pathogensReviews in Medical Microbiology, 1996
- Interaction of the bacterial protein toxin α‐haemolysin with model membranes: protein binding does not always lead to lytic activityFEBS Letters, 1995
- α‐Haemolysin from E. coli purification and self‐aggregation propertiesFEBS Letters, 1991
- The repeat domain of Escherichia coli haemolysin (HlyA) is responsible for its Ca2+-dependent binding to erythrocytesMolecular Genetics and Genomics, 1988
- Purification of α-hemolysin from an overproducing E. coli strainMolecular Genetics and Genomics, 1985